NMR Study of the Positions of His-12 and His-119 in the Ribonuclease A-Uridine Vanadate Complex
PubMed Central® ID
The binding of uridine vanadate to ribonuclease A has been investigated by one- and two-dimensional 1H NMR. The homonuclear Nuclear Overhauser and exchange spectroscopy spectrum of the uridine vanadate/RNase A complex exhibits cross peaks between both the C5H and C6H protons of uridine vanadate and the H epsilon 1 proton of His-12 of ribonuclease A. These cross peaks suggest that the H epsilon 1 proton of His-12 is in the vicinity of the uracil base of uridine vanadate, as observed in the crystallographic structure of the uridine vanadate/RNase A complex. However, no cross peaks are observed between the C5H and C6H protons of uridine vanadate and the H epsilon 1 proton of His-119 of ribonuclease A, although they were predicted based upon the distances calculated from coordinates of the crystallographic structure of the complex. These results suggest that there is a significant difference between the positioning of the His-119 side chain in the solution and in the crystallographic structures.
Amino acid sequence, binding sites, histidine, magnetic resonance spectroscopy, protein conformation, ribonuclease, pancreatic, uridine, vanadates
Veenstra, Timothy D. and Lee, L., "NMR Study of the Positions of His-12 and His-119 in the Ribonuclease A-Uridine Vanadate Complex" (1994). Pharmaceutical Sciences Faculty Publications. 538.